{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T12:05:57Z","timestamp":1790165157902,"version":"4.1.0"},"reference-count":33,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":2161,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2003,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Animal toxins are small proteins built on the basis of a few disulfide bonded frameworks. Because of their high variability in sequence and biologic function, these proteins are now used as templates for protein engineering. Here we report the extensive characterization of the structure and dynamics of two toxin folds, the \u201cthree\u2010finger\u201d fold and the short \u03b1\/\u03b2 scorpion fold found in snake and scorpion venoms, respectively. These two folds have a very different architecture; the short \u03b1\/\u03b2 scorpion fold is highly compact, whereas the \u201cthree\u2010finger\u201d fold is a \u03b2 structure presenting large flexible loops. First, the crystal structure of the snake toxin \u03b1 was solved at 1.8\u2010\u00c5 resolution. Then, long molecular dynamics simulations (10 ns) in water boxes of the snake toxin \u03b1 and the scorpion charybdotoxin were performed, starting either from the crystal or the solution structure. For both proteins, the crystal structure is stabilized by more hydrogen bonds than the solution structure, and the trajectory starting from the X\u2010ray structure is more stable than the trajectory started from the NMR structure. The trajectories started from the X\u2010ray structure are in agreement with the experimental NMR and X\u2010ray data about the protein dynamics. Both proteins exhibit fast motions with an amplitude correlated to their secondary structure. In contrast, slower motions are essentially only observed in toxin \u03b1. The regions submitted to rare motions during the simulations are those that exhibit millisecond time\u2010scale motions. Lastly, the structural variations within each fold family are described. The localization and the amplitude of these variations suggest that the regions presenting large\u2010scale motions should be those tolerant to large insertions or deletions.<\/jats:p>","DOI":"10.1110\/ps.0227703","type":"journal-article","created":{"date-parts":[[2003,1,21]],"date-time":"2003-01-21T20:48:06Z","timestamp":1043182086000},"page":"266-277","source":"Crossref","is-referenced-by-count":17,"title":["Motions and structural variability within toxins: Implication for their use as scaffolds for protein engineering"],"prefix":"10.1002","volume":"12","author":[{"given":"Bernard","family":"Gilquin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marjorie","family":"Bourgoin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren\u00e9e","family":"M\u00e9nez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie\u2010H\u00e9l\u00e8ne","family":"Le Du","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denis","family":"Servent","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophie","family":"Zinn\u2010Justin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e9","family":"M\u00e9nez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0134(19990901)36:4<447::AID-PROT8>3.0.CO;2-E"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1720574"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/9780470141205"},{"key":"e_1_2_9_5_1","volume-title":"A system for X\u2010ray crystallography and NMR.","author":"Br\u00fcnger A.T.","year":"1992"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00211787"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00684a012"},{"key":"e_1_2_9_8_1","first-page":"131","article-title":"Functional anatomy of scorpion toxins affecting sodium channels","volume":"17","author":"Gordon D.","year":"1998","journal-title":"J. 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